Influence of different assignment conditions on the determination of symmetric homodimeric structures with ARIA.
The ambiguous restraint for iterative assignment (ARIA) approach for NMR structure calculation is evaluated for symmetric homodimeric proteins by assessing the effect of several data analysis and assignment methods on the structure quality. In particular, we study the effects of network anchoring and spin-diffusion correction. The spin-diffusion correction improves the protein structure quality systematically, whereas network anchoring enhances the assignment efficiency by speeding up the convergence and coping with highly ambiguous data. For some homodimeric folds, network anchoring has been proved essential for unraveling both chain and proton assignment ambiguities.
Bardiaux
Benjamin
B
Institut Pasteur, Unite de Bioinformatique Structurale, CNRS URA 2185, Paris, France.
Bernard
Aymeric
A
Rieping
Wolfgang
W
Habeck
Michael
M
Malliavin
Thérèse E
TE
Nilges
Michael
M
D000465:Algorithms; D019281:Dimerization; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D015203:Reproducibility of Results
D011506:Proteins